Mitochondrial DNA from <i>Aspergillus nidulans</i>

Perez, Manuel J. Lopez; Turner, Geoffrey

doi:10.1016/0014-5793(75)80248-1

Cited by 21 publications

(3 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, this inflation is minimal and within the error intrinsic to the method. In the slow-growing mycobiont, mitochondrial DNA is probably around 1%, closer to the percent in the filamentous ascomycetes Aspergillus nidulans (Lopez Perez and Turner, 1975) and Neurospora crassa (Luck and Reich, 1964), than to the 5-15% (depending on growth conditions) in the fast-growing yeast Saccharomyces cerevisiae (Fukuhara, 1969;Grimes et al, 1974). In the photobiont Asterochloris, chloroplast and mitochondrial DNA together probably do not exceed 5%, based on values determined for other unicellular algae like Chlamydomonas reinhardtii (Wurtz et al, 1977) and Euglena gracilis (Lyman et al, 1975).…”

Section: Resultsmentioning

confidence: 96%

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

Armaleo

May

2009

Symbiosis

View full text Add to dashboard Cite

Using a method based on quantitative PCR, we determined that the nuclear genome sizes for the mycobiont and photobiont of the lichen Cladonia grayi are 28.6 Mb and 106.7 Mb, respectively. This is the first genome size determination for lichens, and suggests that between 20,000 and 25,000 genes function in C. grayi. The mycobiont genome size is near the middle of the range observed within the Pezizomycota, the subphylum containing all known ascomycete lichen fungi. The genome size of the photobiont (the green alga Asterochloris sp.) is near the lower end of its class, the Trebouxiophyceae. Genomes in this size range can be sequenced at relatively low cost with current pyrosequencing-based methods. The genome sizing method requires very small amounts of precisely quantified DNA and should be applicable to any lichen whose symbionts can be reliably isolated from one another. Since the symbionts used in this project were isolated from soredia, the lichen's vegetative propagules, we also describe a method for the establishment of axenic symbiont cultures from large numbers of soredia.

show abstract

Section: Resultsmentioning

confidence: 96%

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

Armaleo

May

2009

Symbiosis

View full text Add to dashboard Cite

show abstract

“…In the case of Podospora the work was initiated mainly because of the involvement of the mitochondrial DNA in the senescence phenomenon exhibited by this organism [4 -61. Although the number of mitochondrial genes coding for major products seems apriori equivalent in the three species, the mitochondrial chromosome of Podospora (90 x l o 3 bases) [7] is longer than that of Neurospora (60 x lo3 bases) [8] or Aspergillus (33 x lo3 bases) [9,10] and is, in fact, the longest mitochondrial chromosome yet reported (aside from those of plants).…”

Section: A 20 X 103-base Mosaic Gene Identified On the Mitochondrial mentioning

confidence: 95%

A 20 × 10³‐base mosaic gene identified on the mitochondrial chromosome of Podospora anserina

Jamet‐Vierny

Begel

Belcour

1984

European Journal of Biochemistry

View full text Add to dashboard Cite

By DNA sequencing and hybridization experiments we have localized the genes cob and col on the mitochondrial chromosome of Podospora anserina. The positions we have determined for these two genes are different from those previously attributed to them. The presence in the gene col of at least two introns, belonging respectively to class I and II, has been demonstrated. This gene, with a size of about 20 × 103 bases, appears to be the longest known mitochondrial mosaic gene.

show abstract

“…It is quite clear that the smallest-molecular-weight component of the Aspergillus ATPase complex, which binds dicyclohexylcarbodiimide, is of cytoplasmic [30,31]. [14,18].…”

Section: Dicyclohexylcarbodiimide-binding Proteinmentioning

confidence: 99%

Mitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein

Turner

Imam

Küntzel

1979

European Journal of Biochemistry

Self Cite

View full text Add to dashboard Cite

The dicyclohexylcarbodiimide-binding protein of Aspergillus nidulans has been identified as the smallest subunit of the mitochondrial ATPase complex, and has a molecular weight of approximately 8000. It is extractable from whole mitochondria and from the purified enzyme in neutral chloroform/ methanol, contains 30% polar amino acids, and the N-terminal amino acid has been identified as tyrosine. Using a double-labelling technique in the absence and presence of cycloheximide, followed by immunoprecipitation of the enzyme complex with antiserum against Neurospora crassa F1 ATPase, it has been shown that this subunit is synthesized on cytoplasmic ribosomes.Oligomycin-resistant mutants have been isolated in the filamentous Ascomycete Aspergillus nidulans [l ] and mutations in both nuclear and extranuclear genomes have been shown to affect the oligomycin sensitivity of the mitochondria1 ATPase activity [2,3], suggesting the involvement of at least two subunits of the enzyme complex, one nuclearly coded and one extranuclearly coded, in the expression of oligomycin resistance. Furthermore, nuclear-extranuclear interactions have been observed in strains containing mutations in both genomes [3]. In contrast, only extranuclear oligomycin-resistant mutants in Saccharomyces cerevisiae [4,5] and nuclear oligomycin-resistant mutants in Neurospora crassa [6] have been shown to alter the resistance of the ATPase activity of these organisms in vitro.In order to identify the lesions caused by these mutants, and thus the gene-protein relationships, studies on the ATPase complex are essential. Oligomycin is known to inhibit oxidative phosphorylation by acting on the Fo or membrane components of the complex [7]. Dicyclohexylcarbodiimide acts at a nearby site in a similar manner, and shows irreversible binding to one of the FO components [8-111. This hydrophobic polypeptide, referred to as the dicyclohexylcarbodiimide-binding protein, has now been extracted from a number of sources, including the mitochondria of beef heart [ll, 121, S. cerevisiae [13,14] and N . crassa 11.51, the chloroplasts of lettuce [16] and from membranes of Escherichia coli [17]. In all of these species the protein has a molecular weight of

show abstract

Mitochondrial DNA from Aspergillus nidulans

Cited by 21 publications

References 19 publications

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

A 20 × 10³‐base mosaic gene identified on the mitochondrial chromosome of Podospora anserina

Mitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein

Contact Info

Product

Resources

About

Mitochondrial DNA from Aspergillus nidulans

Cited by 21 publications

References 19 publications

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

Sizing the fungal and algal genomes of the lichen Cladonia grayi through quantitative PCR

A 20 × 103‐base mosaic gene identified on the mitochondrial chromosome of Podospora anserina

Mitochondrial ATPase Complex of Aspergillus nidulans and the Dicyclohexylcarbodiimide‐Binding Protein

Contact Info

Product

Resources

About

A 20 × 10³‐base mosaic gene identified on the mitochondrial chromosome of Podospora anserina